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UniProtKB/Swiss-Prot entry P39126


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IDH_BACSU
Primary accession number P39126
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 73)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NADP]
Synonyms IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
Gene name
Name: icd
Synonyms: citC
OrderedLocusNames: BSU29130
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / SMY;
PubMed=8045898 [NCBI, ExPASy, EBI, Israel, Japan]
Jin S., Sonenshein A.L.;
"Identification of two distinct Bacillus subtilis citrate synthase genes.";
J. Bacteriol. 176:4669-4679(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9387221 [NCBI, ExPASy, EBI, Israel, Japan]
Lapidus A., Galleron N., Sorokin A., Ehrlich S.-D.;
"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.";
Microbiology 143:3431-3441(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[4]
PHOSPHORYLATION.
DOI=10.1074/jbc.M107908200; PubMed=11751849 [NCBI, ExPASy, EBI, Israel, Japan]
Singh S.K., Miller S.P., Dean A., Banaszak L.J., LaPorte D.C.;
"Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/phosphatase.";
J. Biol. Chem. 277:7567-7573(2002).
[5]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH CITRATE, AND SUBUNIT.
DOI=10.1074/jbc.M101191200; PubMed=11290745 [NCBI, ExPASy, EBI, Israel, Japan]
Singh S.K., Matsuno K., LaPorte D.C., Banaszak L.J.;
"Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase.";
J. Biol. Chem. 276:26154-26163(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U05257; AAA96342.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF008220; AAC00346.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99118; CAB14873.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I40382; I40382.
RefSeq NP_390791.1; -.
3D structure databases
PDB
1HQS; X-ray; 1.55 A; A/B=1-423.[ExPASy / RCSB / EBI]
PDBsum 1HQS; -.
ModBase P39126.
PTM databases
PhosSite P39126; -.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2909-MON; -.
Organism-specific databases
SubtiList BG10856; icd. [Micado]
Family and domain databases
InterPro IPR004439; IsoCit_DHase_NADP_prok.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF1; NADP_IDH_prok; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00183; prok_nadp_idh; 1.
PROSITE PS00470; IDH_IMDH; 1.
BLOCKS P39126.
Genome annotation databases
GeneID 938183; -.
GenomeReviews AL009126_GR; BSU29130.
KEGG bsu:BSU29130; -.
NMPDR fig|224308.1.peg.2916; -.
Phylogenomic databases
HOGENOM P39126; -.
Genome annotation databases
CMR P39126; BSU29130.
Other
ProtoNet P39126.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   423  423     Isocitrate dehydrogenase [NADP]. PRO_0000083549
NP_BIND   345   351  7     NADP (By similarity). 
METAL   311   311        Magnesium or manganese (By similarity). 
BINDING   95    95        NADP (By similarity). 
BINDING   96    96        Substrate. 
BINDING   104   104        Substrate. 
BINDING   106   106        Substrate. 
BINDING   110   110        Substrate. 
BINDING   120   120        Substrate (By similarity). 
BINDING   144   144        Substrate. 
BINDING   358   358        NADP; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   397   397        NADP (By similarity). 
BINDING   401   401        NADP (By similarity). 
SITE   151   151  1     Critical for catalysis (By similarity). 
SITE   221   221  1     Critical for catalysis (By similarity). 
STRAND   3     5  3      
STRAND   8    10  3      
STRAND   13    15  3      
STRAND   18    25  8      
HELIX   31    50  20      
STRAND   57    60  4      
HELIX   65    71  7      
HELIX   77    86  10      
STRAND   88    91  4      
STRAND   98   102  5      
HELIX   105   112  8      
STRAND   117   123  7      
STRAND   131   133  3      
HELIX   135   137  3      
STRAND   139   145  7      
HELIX   149   152  4      
HELIX   161   173  13      
HELIX   182   184  3      
STRAND   185   193  9      
HELIX   194   211  18      
STRAND   214   220  7      
TURN   222   224  3      
TURN   226   228  3      
HELIX   229   244  16      
HELIX   245   247  3      
STRAND   248   250  3      
HELIX   251   275  25      
STRAND   279   285  7      
HELIX   286   295  10      
HELIX   297   299  3      
STRAND   301   305  5      
HELIX   307   320  14      
TURN   324   326  3      
STRAND   328   332  5      
TURN   334   336  3      
STRAND   339   344  6      
HELIX   349   351  3      
TURN   352   355  4      
HELIX   360   373  14      
HELIX   376   391  16      
HELIX   397   400  4      
STRAND   403   405  3      
HELIX   411   420  10      
Sequence information
Length: 423 AA [This is the length of the unprocessed precursor] Molecular weight: 46418 Da [This is the MW of the unprocessed precursor] CRC64: CC69E694EB66D0D8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQGEKITVS NGVLNVPNNP IIPFIEGDGT GPDIWNAASK VLEAAVEKAY KGEKKITWKE 

        70         80         90        100        110        120 
VYAGEKAYNK TGEWLPAETL DVIREYFIAI KGPLTTPVGG GIRSLNVALR QELDLFVCLR 

       130        140        150        160        170        180 
PVRYFTGVPS PVKRPEDTDM VIFRENTEDI YAGIEYAKGS EEVQKLISFL QNELNVNKIR 

       190        200        210        220        230        240 
FPETSGIGIK PVSEEGTSRL VRAAIDYAIE HGRKSVTLVH KGNIMKFTEG AFKNWGYELA 

       250        260        270        280        290        300 
EKEYGDKVFT WAQYDRIAEE QGKDAANKAQ SEAEAAGKII IKDSIADIFL QQILTRPNEF 

       310        320        330        340        350        360 
DVVATMNLNG DYISDALAAQ VGGIGIAPGA NINYETGHAI FEATHGTAPK YAGLDKVNPS 

       370        380        390        400        410        420 
SVILSGVLLL EHLGWNEAAD LVIKSMEKTI ASKVVTYDFA RLMDGATEVK CSEFGEELIK 


NMD 

P39126 in FASTA format

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